KCRU_CHICK
ID KCRU_CHICK Reviewed; 417 AA.
AC P70079; Q90782;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Creatine kinase U-type, mitochondrial;
DE EC=2.7.3.2;
DE AltName: Full=Acidic-type mitochondrial creatine kinase;
DE Short=Mia-CK;
DE AltName: Full=Ubiquitous mitochondrial creatine kinase;
DE Short=U-MtCK;
DE Flags: Precursor;
GN Name=CKMT1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=White leghorn; TISSUE=Brain, and Liver;
RX PubMed=8662608; DOI=10.1074/jbc.271.20.11920;
RA Muehlebach S.M., Wirz T., Braendle U., Perriard J.-C.;
RT "Evolution of the creative kinases. The chicken acidic type mitochondrial
RT creatine kinase gene as the first nonmammalian gene.";
RL J. Biol. Chem. 271:11920-11929(1996).
RN [2]
RP PROTEIN SEQUENCE OF 40-68.
RC TISSUE=Brain;
RX PubMed=2831887; DOI=10.1016/0006-291x(88)90608-0;
RA Hossle J.P., Schlegel J., Wegmann G., Wyss M., Boehlen P.,
RA Eppenberger H.M., Wallimann T., Perriard J.-C.;
RT "Distinct tissue specific mitochondrial creatine kinases from chicken brain
RT and striated muscle with a conserved CK framework.";
RL Biochem. Biophys. Res. Commun. 151:408-416(1988).
CC -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP
CC and various phosphogens (e.g. creatine phosphate). Creatine kinase
CC isoenzymes play a central role in energy transduction in tissues with
CC large, fluctuating energy demands, such as skeletal muscle, heart,
CC brain and spermatozoa.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + creatine = ADP + H(+) + N-phosphocreatine;
CC Xref=Rhea:RHEA:17157, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57947, ChEBI:CHEBI:58092, ChEBI:CHEBI:456216; EC=2.7.3.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10029};
CC -!- SUBUNIT: Exists as an octamer composed of four MTCK homodimers.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC protein; Intermembrane side.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and gut, weakly in
CC testis. Also found in cell bodies of neural cells of the gray matter.
CC -!- MISCELLANEOUS: Mitochondrial creatine kinase binds cardiolipin.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
CC ProRule:PRU00843}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA65266.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X96403; CAA65267.1; -; Genomic_DNA.
DR EMBL; X96402; CAA65266.1; ALT_INIT; Genomic_DNA.
DR EMBL; X95526; CAA64778.1; -; Genomic_DNA.
DR AlphaFoldDB; P70079; -.
DR SMR; P70079; -.
DR STRING; 9031.ENSGALP00000013585; -.
DR PaxDb; P70079; -.
DR VEuPathDB; HostDB:geneid_374002; -.
DR eggNOG; KOG3581; Eukaryota.
DR InParanoid; P70079; -.
DR PhylomeDB; P70079; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; IBA:GO_Central.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.135.10; -; 1.
DR InterPro; IPR000749; ATP-guanido_PTrfase.
DR InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR InterPro; IPR022413; ATP-guanido_PTrfase_N.
DR InterPro; IPR036802; ATP-guanido_PTrfase_N_sf.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR11547; PTHR11547; 1.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR Pfam; PF02807; ATP-gua_PtransN; 1.
DR SUPFAM; SSF48034; SSF48034; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Kinase; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2831887"
FT CHAIN 40..417
FT /note="Creatine kinase U-type, mitochondrial"
FT /id="PRO_0000016593"
FT DOMAIN 44..131
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT DOMAIN 158..400
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 161..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 353..358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
SQ SEQUENCE 417 AA; 47104 MW; ED9B982764153D2C CRC64;
MASTFARALS ARRSAGLLAM VGAGSLAAGF LLARDTVSAG ERQRRRYPPS AEYPDLRKHN
NCMASNLTPA IYARLCDKAT PNGWTLDQCI QTGVDNPGHP FIKTVGMVAG DEETYEVFAE
LFDPVIQERH NGYNPRTMKH VTDLDASKIK FGHFDERYVL SSRVRTGRSI RGLSLPPACT
RAERREVEKV TVEALNGLTG DLSGRYYRLS EMTEKEQQQL IDDHFLFDKP VSPSLTAAGM
ARDWPDARGI WHNNEKTFLI WINEEDHTRV ISMEKGGNMK RVFERFCRGL KEVERLIQER
GWEFMWNERL GYILTCPSNL GTGLRAGVHI KLPLLSKDSR FPKILENLRL QKRGTGGVDT
AATANVFDIS NLDRLGKSEV ELVQLVIDGV NYLIDCERRL EKGQDIRIPS PVPQFRH
